Tissue specificity of non‐histone chromatin phosphoproteins

Platz, Robert D.; Kish, Valerie M.; Kleinsmith, Lewis J.

doi:10.1016/0014-5793(70)80589-0

Cited by 85 publications

(17 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our knowledge of even the elementary properties of these chromatin acidic proteins, however, is meager due to the technical difficulties encountered in their isolation, fractionation, and characterization (2). Chromatin a9eidic proteins, isolated by various methods from many cell types, are heterogeneous and tissue and species specific (3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17) , and confer tissue and species specificity to the chromatin template in transcription (8,(18)(19)(20). The latter observations strongly indicate a gene regulatory role for at least some of the nonhistone acidic proteins.…”

mentioning

confidence: 99%

Some Binding Parameters of Chromatin Acidic Proteins with High Affinity for Deoxyribonucleic Acid

Patel¹,

Thomas²

1973

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

A fraction of chromatin acidic protein from rat liver, predominantly comprised of low-molecular-weight species, showed highest in vitro affinity for DNA when compared with other fractions of nuclear acidic protein. Maximum binding of this protein fraction was observed at physiological ionic strength of 0.14 M NaCi and DNA/protein ratio > 1. Comparison of their binding to homologous and heterologous DNAs showed partial species specificity. All molecular species of this protein fraction appear to bind to DNA.A prerequisite feature of proteins involved in the structure and function of the genome is the capacity to interact specifically with deoxyribonucleic acid. In eukaryotes, histones, a class of basic proteins, which have been recognized as DNA-associated components of the chromatin, have been investigated intensely (ref. 1 for recent review); and yet, their exact nuclear function has not been clearly defined. In addition to histones, the chromatin also contains a variable, but significant, amount of acidic proteins. Our knowledge of even the elementary properties of these chromatin acidic proteins, however, is meager due to the technical difficulties encountered in their isolation, fractionation, and characterization (2). Chromatin a9eidic proteins, isolated by various methods from many cell types, are heterogeneous and tissue and species specific (3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17) , and confer tissue and species specificity to the chromatin template in transcription (8,(18)(19)(20). The latter observations strongly indicate a gene regulatory role for at least some of the nonhistone acidic proteins. Some recent reports have shown in vitro binding of some chromatin acidic proteins to DNA in a species-specific manner (11,21). These observations are analogous to those in prokaryotes, where gene regulatory proteins interact specifically with DNA (22,23). A study of nuclear proteins, in particular the nonhistone acidic proteins of chromatin with high affinity for DNA, is, therefore, of interest in connection with their possible role in chromatin structure and/or in regulation of replication and transcription.Recently the isolation from rat-liver chromatin of a class of acidic proteins with high affinity for nucleohistone and DNA and predominantly comprised of low-molecular-weight species was reported from this laboratory (14). These proteins are distinct from other fractions of nuclear acidic proteins and from chromatin acidic proteins that bind DNA reported by Acidic Proteins with High others. In the present study we report on some of the in vitro DNA binding parameters of these acidic proteins. MATERIALS AND METHODSIsolation of Nuclei. Male Sprague-Dawley rats (200-250 g) were kept on Purina chow freely until 24 hr before they were killed by decapitation. Livers were removed immediately, washed with ice-cold 0.25 M sucrose-3 mM CaCl2, and processed to purify nuclei by the method of Pogo et al. (24), with additional filtration of tissue homogenates through Miracloth and substitution of Mg...

show abstract

mentioning

confidence: 99%

Some Binding Parameters of Chromatin Acidic Proteins with High Affinity for Deoxyribonucleic Acid

Patel¹,

Thomas²

1973

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…Although tissue specificity of nonhistone phosphoproteins has been noted [7,20], this and another study [21 ] suggest limited qualitative tissue specificity. However, this system probably cannot detect tissue specific gene control proteins present in very low concentrations.…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of non‐histone chromatin proteins in normal and regenerating rat liver, novikoff hepatoma and rat heart

et al. 1976

View full text Add to dashboard Cite

“…The nuclei were isolated (Platz et al, 1970) from brains of adult rats. Microscopically it was confirmed that the purified nuclei contained both larger neuronal and smaller glial nuclei.…”

Section: Methodsmentioning

confidence: 99%

The Soluble Proteins and RNA of Rat Brain Nuclei

Jokela

Piha

1972

International Journal of Neuroscience

View full text Add to dashboard Cite

We have tried to characterize some soluble proteins obtained by saline extraction from purified brain nuclei. It is impossible to say whether these soluble nuclear proteins have any role in information transfer from the functional point of view. However, these proteins may have a role in the information transfer at a genetic lever (transcription). In the regulations of gene activity these nuclear proteins may function as single polypeptide chains of polypeptide chain aggregates.

show abstract

Tissue specificity of non‐histone chromatin phosphoproteins

Cited by 85 publications

References 13 publications

Some Binding Parameters of Chromatin Acidic Proteins with High Affinity for Deoxyribonucleic Acid

Some Binding Parameters of Chromatin Acidic Proteins with High Affinity for Deoxyribonucleic Acid

Phosphorylation of non‐histone chromatin proteins in normal and regenerating rat liver, novikoff hepatoma and rat heart

The Soluble Proteins and RNA of Rat Brain Nuclei

Contact Info

Product

Resources

About